1.
What is metabolism?
Correct Answer
A. All of the chemical reactions in an organism
Explanation
Metabolism refers to all of the chemical reactions that occur within an organism. This includes processes such as breaking down complex molecules into simpler ones (polymer to monomer reactions) which release ATP, as well as building up complex molecules from simpler ones (monomer to polymer reactions) which require ATP. Therefore, the correct answer is "All of the chemical reactions in an organism".
2.
What is catabolism?
Correct Answer
B. Polymer to monomer reactions that release ATP and break down
Explanation
Catabolism refers to the process of breaking down complex molecules, such as polymers, into simpler molecules, known as monomers. This process releases energy in the form of ATP. Therefore, the correct answer is "Polymer to monomer reactions that release ATP and break down."
3.
What is anabolism?
Correct Answer
C. Monomer to polymer reactions that require ATP and build up
Explanation
Anabolism refers to the metabolic process in which smaller molecules, known as monomers, are combined to form larger molecules, known as polymers. This process requires the input of energy in the form of ATP and is responsible for building up complex molecules in an organism. Therefore, the correct answer is "Monomer to polymer reactions that require ATP and build up."
4.
What is adenosine made of?
Correct Answer
D. Adenine and ribose
Explanation
Adenosine is a nucleoside composed of adenine and ribose. Adenine is one of the four nitrogenous bases found in DNA and RNA, while ribose is a pentose sugar. Together, they form adenosine, which plays a crucial role in various biological processes, including energy transfer and signal transduction.
5.
How many high energy bonds does ATP have?
Correct Answer
C. 2
Explanation
ATP (adenosine triphosphate) is a molecule that stores and releases energy for cellular processes. It contains two high energy bonds between its phosphate groups. These bonds are easily broken, releasing energy when needed for various cellular activities. Therefore, the correct answer is 2.
6.
How many high energy bonds does ADP have?
Correct Answer
B. 1
Explanation
ADP (adenosine diphosphate) has one high energy bond. This bond is found between the second and third phosphate groups in the molecule. When this bond is broken, energy is released and ADP is converted into ATP (adenosine triphosphate), which is the primary energy currency of cells.
7.
How many high energy bonds does AMP have?
Correct Answer
A. 0
Explanation
AMP, or adenosine monophosphate, does not have any high energy bonds. High energy bonds are typically found in molecules such as ATP (adenosine triphosphate), where the energy stored in these bonds is readily available for cellular processes. In AMP, the phosphate group is only attached to the ribose sugar by a single bond, making it a low-energy molecule. Therefore, the correct answer is 0.
8.
Are enzymes proteins?
Correct Answer
B. All of them are, but not all proteins are enzymes
Explanation
The answer "All of them are, but not all proteins are enzymes" is correct because enzymes are a type of protein. However, not all proteins are enzymes. Proteins have various functions in the body, and while enzymes are proteins, there are other types of proteins that do not have enzymatic activity.
9.
What do enzymes do?
Correct Answer
B. Speed up chemical reaction
Explanation
Enzymes are biological catalysts that speed up chemical reactions in living organisms. They do this by lowering the activation energy required for a reaction to occur, allowing it to happen more quickly. Enzymes themselves are not consumed or changed during the reaction, making them highly efficient in facilitating various metabolic processes.
10.
What is the substrate?
Correct Answer
E. A and D
Explanation
The substrate refers to the specific molecule or molecules that are acted upon by an enzyme. In this case, the correct answer is A and D, which means that the substrate can be either the reactant(s) or the products of the reaction. This implies that the enzyme can either act on the reactant(s) to produce the product(s), or it can act on the product(s) to convert them back into the reactant(s).
11.
What is the part of enzyme where the substrate is given an induced (tight) fit?
Correct Answer
D. Active site
Explanation
The active site of an enzyme is the part where the substrate molecule binds and undergoes a chemical reaction. It provides a specific environment that allows the substrate to fit tightly and interact with the enzyme's active site residues. This induced fit ensures that the enzyme and substrate form a stable complex, facilitating the catalytic reaction.
12.
How do enzymes speed up chemical reactions?
Correct Answer
E. B and C
Explanation
Enzymes speed up chemical reactions by lowering the activation energy required for the reaction to occur. They do this by binding to the reactant molecules and bringing them closer together, allowing them to interact more easily. Additionally, enzymes can also provide a microenvironment that is conducive to the reaction, such as a specific pH or temperature. Therefore, the correct answer is B and C, as both lowering the activation energy and providing a favorable environment are ways in which enzymes speed up chemical reactions.
13.
What happens if you denature an enzyme?
Correct Answer
C. Change shape of active site, no longer works
Explanation
Denaturing an enzyme refers to the process of altering its structure, usually through the application of heat or extreme pH levels. This alteration in structure leads to a change in the shape of the enzyme's active site. Since the active site is responsible for binding to the substrate and catalyzing the reaction, any change in its shape will disrupt the enzyme's ability to function properly. Therefore, when an enzyme is denatured, it no longer works.
14.
What is an enzyme inhibitor?
Correct Answer
B. Something that slows down the enzyme
Explanation
An enzyme inhibitor is a substance that slows down the activity of an enzyme. It does not completely stop the enzyme or denature it, but rather reduces its ability to catalyze a reaction. Inhibitors can bind to the active site of the enzyme or to other sites, causing a change in the enzyme's shape or interfering with its ability to bind to the substrate. This ultimately decreases the rate of the enzymatic reaction, allowing for regulation and control of biochemical processes in the body.
15.
What is a competitive inhibitor?
Correct Answer
A. An inhibitor that moves into active site of enzyme
Explanation
A competitive inhibitor is a type of inhibitor that binds to the active site of an enzyme, preventing the substrate from binding and inhibiting the enzyme's activity. It competes with the substrate for binding to the active site. This type of inhibition can be overcome by increasing the concentration of the substrate.
16.
How do you overcome the inhibitor?
Correct Answer
D. Increase concentration of substrate
Explanation
Increasing the concentration of substrate can help overcome the inhibitor because the inhibitor binds to the enzyme, preventing it from binding to the substrate and catalyzing the reaction. By increasing the concentration of substrate, there will be a higher chance of the substrate molecules binding to the enzyme instead of the inhibitor, allowing the reaction to proceed. This effectively reduces the impact of the inhibitor and allows the enzyme to function more effectively.
17.
What is non-competitive inhibitor?
Correct Answer
E. B and C
Explanation
A non-competitive inhibitor is an inhibitor that does not bind to the active site of an enzyme. Instead, it binds to a different site on the enzyme, called the non-active site, and causes a change in the conformation of the protein. This change in conformation prevents the enzyme from functioning properly. In some cases, a non-competitive inhibitor can act as a poison, causing harm to the organism. Therefore, the correct answer is B and C.
18.
What are allosteric enzymes?
Correct Answer
C. Enzymes that change shape to toggle between active and inactive
Explanation
Allosteric enzymes are enzymes that change shape in order to switch between active and inactive states. This change in shape is triggered by the binding of a molecule, called an allosteric regulator, to a specific site on the enzyme that is separate from the active site. This binding causes a conformational change in the enzyme, which either enhances or inhibits its activity. Allosteric enzymes play a crucial role in regulating metabolic pathways and maintaining homeostasis in cells.
19.
How do allosteric enzymes become active?
Correct Answer
A. Activator attaches
Explanation
Allosteric enzymes become active when an activator attaches to them. This attachment causes a conformational change in the enzyme's structure, leading to an increase in its catalytic activity. The activator molecule binds to a specific regulatory site on the enzyme, which is distinct from the active site where the substrate binds. This allosteric regulation allows for the fine-tuning of enzyme activity in response to cellular needs.
20.
How do allosteric enzymes become inactive?
Correct Answer
B. Inhibitor attaches
Explanation
When an inhibitor attaches to an allosteric enzyme, it causes a conformational change in the enzyme's active site. This change prevents the substrate from binding to the enzyme, rendering it inactive. By inhibiting the binding of the substrate, the inhibitor effectively shuts down the enzyme's catalytic activity.